Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions
K01462
-
3.5.1.88
0.00000002161
57.0
MMS1_k127_1381329_0
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
K03046
-
2.7.7.6
0.0
1113.0
MMS1_k127_1381329_1
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
K03043
-
2.7.7.6
0.0
1090.0
MMS1_k127_1381329_10
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons
K03625
-
-
0.0000000000000000000000001117
119.0
MMS1_k127_1381329_12
Endonuclease containing a URI domain
K07461
-
-
0.00000000000000001238
84.0
MMS1_k127_1381329_13
KH domain
-
-
-
0.0000000000002072
74.0
MMS1_k127_1381329_14
Belongs to the bacterial ribosomal protein bS16 family
K02959
-
-
0.00000000000321
74.0
MMS1_k127_1381329_15
-
-
-
-
0.00000003243
59.0
MMS1_k127_1381329_16
structural constituent of ribosome
K02911
-
-
0.0000003738
56.0
MMS1_k127_1381329_17
COG3893 Inactivated superfamily I helicase
-
-
-
0.0006629
48.0
MMS1_k127_1381329_2
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre- crRNA and tracrRNA of type II CRISPR loci if present in the organism
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre- initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions
K03530
-
-
0.0000000000000000000000004243
106.0
MMS1_k127_1663316_14
LysE type translocator
-
-
-
0.0000003506
60.0
MMS1_k127_1663316_2
Single-strand DNA-specific exonuclease, C terminal domain
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions
K01507
-
3.6.1.1
0.000000000000000000000000000000000000000000195
165.0
MMS1_k127_1663316_8
PFAM ComEC Rec2-related protein
K02238
-
-
0.00000000000000000000000000000000000002789
161.0
MMS1_k127_1663316_9
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P)
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre- initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex
K02518
-
-
0.0000000000318
67.0
MMS1_k127_1685465_4
Belongs to the bacterial ribosomal protein bL36 family
K02919
-
-
0.0000009963
51.0
MMS1_k127_1714789_0
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA
K03072
-
-
0.0000000000000000000000000000000001835
141.0
MMS1_k127_1871471_4
Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate
K01491
-
1.5.1.5,3.5.4.9
0.0000000000000000000000000008639
123.0
MMS1_k127_1871471_5
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR)
-
-
-
0.00001798
55.0
MMS1_k127_1871471_6
Nad-dependent epimerase dehydratase
K08679
-
5.1.3.6
0.0004124
52.0
MMS1_k127_2094198_0
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance
Necessary for normal cell division and for the maintenance of normal septation
K03978
-
-
0.000000000000000000000000000000000001824
145.0
MMS1_k127_2113188_8
Cytochrome b subunit of the bc complex
K00412,K15879
-
-
0.000000000000000000000001036
115.0
MMS1_k127_2113188_9
-
-
-
-
0.000000000000001443
85.0
MMS1_k127_2216205_0
amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
amino acids such as threonine, to avoid such errors, it has a posttransfer editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner
K01873
-
6.1.1.9
4.558e-205
661.0
MMS1_k127_2277343_1
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and or decay
Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family
K03585
-
-
0.0000007762
62.0
MMS1_k127_232072_9
Domain of unknown function (DUF378)
K09779
-
-
0.000001469
53.0
MMS1_k127_2351755_0
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 uvrA and 2 uvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by uvrB, the uvrA molecules dissociate
K03701
-
-
4.256e-289
915.0
MMS1_k127_2351755_1
nucleotide-excision repair
K03702,K08999
-
-
7.937e-235
745.0
MMS1_k127_2351755_11
Peptidyl-prolyl cis-trans
K01802,K03772
-
5.2.1.8
0.00000000000000000000000000000004563
130.0
MMS1_k127_2351755_12
Putative diguanylate phosphodiesterase
-
-
-
0.0000000000000000000000000003143
125.0
MMS1_k127_2351755_13
adenosine 5'-monophosphoramidase activity
-
-
-
0.00000000000000000000003277
105.0
MMS1_k127_2351755_2
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA)
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine)
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision
K03703
-
-
0.0000000000000000000000000000000000000000000557
175.0
MMS1_k127_2351755_9
Belongs to the D-alanine--D-alanine ligase family
K01921
-
6.3.2.4
0.00000000000000000000000000000000000000001758
166.0
MMS1_k127_236597_0
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
Catalyzes the reductive methylation of 2'-deoxyuridine- 5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site
K02884
-
-
0.000000000000000004067
91.0
MMS1_k127_2576121_21
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA
K07447
-
-
0.00000000000000002006
87.0
MMS1_k127_2576121_22
-
-
-
-
0.00000000001205
67.0
MMS1_k127_2576121_23
TIGRFAM type IV pilus assembly protein PilM
K02662
-
-
0.00000000001561
76.0
MMS1_k127_2576121_24
Cytidine and deoxycytidylate deaminase zinc-binding region
K01493
-
3.5.4.12
0.000000001735
65.0
MMS1_k127_2576121_26
MazG nucleotide pyrophosphohydrolase
-
-
-
0.000001716
55.0
MMS1_k127_2576121_27
Binds directly to 16S ribosomal RNA
K02968
-
-
0.00002038
50.0
MMS1_k127_2576121_29
SecE/Sec61-gamma subunits of protein translocation complex
K03073
-
-
0.0002689
46.0
MMS1_k127_2576121_3
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids
Responsible for synthesis of pseudouridine from uracil
K06180
-
5.4.99.23
0.0000000000000000000000000000000000000000003506
167.0
MMS1_k127_2576121_8
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors
K02867
-
-
0.000000000000000000000000000000000000000002719
159.0
MMS1_k127_2576121_9
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln)
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln)
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate
K01007
-
2.7.9.2
2.648e-280
883.0
MMS1_k127_2595828_10
Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair
K01356
-
3.4.21.88
0.00000000000000000000000000588
119.0
MMS1_k127_2595828_22
COG1028 Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln)
K02435
-
6.3.5.6,6.3.5.7
0.0000001858
57.0
MMS1_k127_2595828_35
-
-
-
-
0.00001274
51.0
MMS1_k127_2595828_36
Helix-turn-helix domain
-
-
-
0.00001996
51.0
MMS1_k127_2595828_37
-
-
-
-
0.00005974
51.0
MMS1_k127_2595828_38
general secretion pathway protein
K02456
-
-
0.0001288
50.0
MMS1_k127_2595828_4
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln)
Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA
K02965
-
-
0.0000000000000000000000002866
109.0
MMS1_k127_2604698_3
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits
K02112
-
3.6.3.14
2.035e-201
636.0
MMS1_k127_2698163_10
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex
it plays a direct role in the translocation of protons across the membrane
K02108
-
-
0.0000000000000000000000000000000000000000003472
168.0
MMS1_k127_2698163_12
SWIB/MDM2 domain
-
-
-
0.00000000000000000000000000000009649
132.0
MMS1_k127_2698163_13
HD domain
-
-
-
0.00000000000000000000000006554
114.0
MMS1_k127_2698163_14
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation
ATP synthase, delta epsilon subunit, beta-sandwich domain protein
K02114
-
-
0.000000001412
61.0
MMS1_k127_2698163_17
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation
K02109
-
-
0.000000005768
64.0
MMS1_k127_2698163_18
PFAM Di-glucose binding within endoplasmic reticulum
-
-
-
0.00000002266
67.0
MMS1_k127_2698163_19
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth
K03086
-
-
0.0001084
54.0
MMS1_k127_2698163_2
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance
K02881
-
-
0.00000000000000000000000000002962
120.0
MMS1_k127_2825315_11
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism
K00939
-
2.7.4.3
0.00000000000000000000000008044
113.0
MMS1_k127_2825315_12
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits
K02931
-
-
0.0000000000000000000000001056
109.0
MMS1_k127_2825315_13
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7 L12 stalk, and near the tRNA binding site of the peptidyltransferase center
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism
K03111
-
-
0.000000000000000000000000000000002363
138.0
MMS1_k127_2840227_3
AI-2E family transporter
-
-
-
0.00000000000000009176
92.0
MMS1_k127_2840227_4
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit
K02963
-
-
0.00000005589
60.0
MMS1_k127_2847020_0
amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates
Part of the ABC transporter FtsEX involved in cellular division
K09811
-
-
0.000000000000000000000000001225
124.0
MMS1_k127_545447_5
Domain of unknown function (DUF389)
-
-
-
0.00000000000000000000002052
109.0
MMS1_k127_545447_6
Cytochrome b(N-terminal)/b6/petB
-
-
-
0.0000000000000000001826
96.0
MMS1_k127_545447_7
Rhodanese Homology Domain
-
-
-
0.00000000000000006612
86.0
MMS1_k127_545447_8
Major facilitator Superfamily
-
-
-
0.0001042
54.0
MMS1_k127_63313_0
Heat shock 70 kDa protein
K04043
-
-
2.706e-232
734.0
MMS1_k127_63313_1
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp Asn)
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves
K05896
-
-
0.0000000000000000000000000894
116.0
MMS1_k127_63313_11
Ribosomal protein L17
K02879
-
-
0.0000000000000000000000001686
110.0
MMS1_k127_63313_12
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly
K02871
-
-
0.000000000000000000005643
96.0
MMS1_k127_63313_15
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves
ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins
K01358
-
3.4.21.92
0.0000000008137
69.0
MMS1_k127_657155_5
DUF167
K09131
-
-
0.0000002007
55.0
MMS1_k127_657155_6
-
-
-
-
0.000776
48.0
MMS1_k127_679632_0
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE
K03695
-
-
3.178e-291
919.0
MMS1_k127_679632_1
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II)
Belongs to the bacterial ribosomal protein bL27 family
K02899
-
-
0.0000002931
52.0
MMS1_k127_692353_0
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue
K02654
-
3.4.23.43
0.000000000000000000000008254
111.0
MMS1_k127_692353_3
PFAM Type II secretion system protein E
K02669
-
-
0.00000372
50.0
MMS1_k127_692353_4
general secretion pathway protein
K02456,K02650
-
-
0.0000148
54.0
MMS1_k127_692353_5
Pfam:N_methyl_2
-
-
-
0.0001577
50.0
MMS1_k127_824008_0
ribonucleoside-diphosphate reductase activity
K00525,K21636
-
1.1.98.6,1.17.4.1
4.323e-294
923.0
MMS1_k127_824008_1
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane
K03980
-
-
0.000000000000000000000000003381
128.0
MMS1_k127_824008_3
tetratricopeptide repeat
-
-
-
0.0000005971
63.0
MMS1_k127_862975_0
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome
K02355
-
-
4.693e-269
847.0
MMS1_k127_862975_1
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit
K02906
-
-
0.000000000000000000000000000000000000000004431
163.0
MMS1_k127_862975_14
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase
K02356
-
-
0.000000000000000000000000000002564
127.0
MMS1_k127_863496_1
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage
K03553
-
-
0.000000000000000005537
86.0
MMS1_k127_863496_2
belongs to the sigma-70 factor family, ECF subfamily
K03088
-
-
0.0000000007036
69.0
MMS1_k127_863662_0
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation
K02935
-
-
0.000000000000000000000000000000000228
138.0
MMS1_k127_863662_1
Lecithin:cholesterol acyltransferase
-
-
-
0.000000006291
70.0
MMS1_k127_863662_2
-O-antigen
-
-
-
0.0000001646
64.0
MMS1_k127_863662_3
transcriptional
-
-
-
0.0000288
53.0
MMS1_k127_863662_4
Conserved TM helix
-
-
-
0.0001078
52.0
MMS1_k127_863662_5
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors
K02864
-
-
0.0009972
48.0
MMS1_k127_873311_0
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner